| Literature DB >> 1547888 |
W C Chan1, B W Bycroft, M L Leyland, L Y Lian, J C Yang, G C Roberts.
Abstract
Subtilin, a 32-amino acid peptide with potent antimicrobial activity, has been isolated from Bacillus subtilis ATCC6633. The chemical structure has been confirmed by the unambiguous sequence-specific assignment of its 1H NMR spectrum. Detailed NMR analysis revealed that subtilin is a rather flexible molecule; the only observed conformational contraints were those imposed by the cyclic structures created by the lanthionine and 3-methyllanthionine residues. These results suggest that in aqueous solution subtilin and the homologous peptide nisin have similar conformations.Entities:
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Year: 1992 PMID: 1547888 DOI: 10.1016/0014-5793(92)80163-b
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124